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Bt Toxin Resistance from Loss of a Putative Carbohydrate-Modifying Enzyme
Joel S. Griffitts,Johanna L. Whitacre,Daniel
E. Stevens,Raffi V. Aroian*
The development of resistance is the main threat to the long-term
use of toxins from Bacillus thuringiensis (Bt) in transgenicplants. Here we report the cloning of a Bt toxin resistance gene,Caenorhabditis elegans bre-5, which encodes a putative
-1,3-galactosyltransferase.Lack of bre-5 in the
intestine led to resistance to the Bt toxinCry5B. Wild-type but not
bre-5 mutant animals were found to uptaketoxin into their
gut cells, consistent with bre-5 mutants lackingtoxin-binding sites on their apical gut. bre-5 mutants
displayedresistance to Cry14A, a Bt toxin lethal to both nematodes andinsects; this indicates that resistance by loss of carbohydratemodification is relevant to multiple Bt toxins.
Section of Cell and Developmental Biology, University of
California, San Diego, La Jolla, CA 92093, USA.
*
To whom correspondence should be addressed. E-mail:
raroian{at}ucsd.edu
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New Positive Regulators of lin-12 Activity in Caenorhabditis elegans Include the BRE-5/Brainiac Glycosphingolipid Biosynthesis Enzyme.
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307, 922-925
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Resistance to a Bacterial Toxin Is Mediated by Removal of a Conserved Glycosylation Pathway Required for Toxin-Host Interactions.
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Bacillus thuringiensis crystal proteins that target nematodes.
J.-Z. Wei, K. Hale, L. Carta, E. Platzer, C. Wong, S.-C. Fang, and R. V. Aroian (2003)
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Insect Resistance to Bacillus thuringiensis: Alterations in the Indianmeal Moth Larval Gut Proteome.
M. Candas, O. Loseva, B. Oppert, P. Kosaraju, and L. A. Bulla Jr. (2003)
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2, 19-28
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Altered Glycosylation of 63- and 68-Kilodalton Microvillar Proteins in Heliothis virescens Correlates with Reduced Cry1 Toxin Binding, Decreased Pore Formation, and Increased Resistance to Bacillus thuringiensis Cry1 Toxins.
J. L. Jurat-Fuentes, F. L. Gould, and M. J. Adang (2002)
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Loss of the membrane anchor of the target receptor is a mechanism of bioinsecticide resistance.
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99, 5830-5835
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Heliothis virescens and Manduca sexta Lipid Rafts Are Involved in Cry1A Toxin Binding to the Midgut Epithelium and Subsequent Pore Formation.
M. Zhuang, D. I. Oltean, I. Gomez, A. K. Pullikuth, M. Soberon, A. Bravo, and S. S. Gill (2002)
J. Biol. Chem.
277, 13863-13872
|Abstract »|Full Text »|PDF »
-1,3-galactosyltransferase. Lack of bre-5 in the
intestine led to resistance to the Bt toxin Cry5B. Wild-type but not
bre-5 mutant animals were found to uptake toxin into their
gut cells, consistent with bre-5 mutants lacking toxin-binding sites on their apical gut. bre-5 mutants
displayed resistance to Cry14A, a Bt toxin lethal to both nematodes and insects; this indicates that resistance by loss of carbohydrate modification is relevant to multiple Bt toxins.
